期刊
STRUCTURE
卷 18, 期 3, 页码 343-353出版社
CELL PRESS
DOI: 10.1016/j.str.2010.01.002
关键词
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资金
- Binational Science Foundation [2005209]
- Kimmelman Center for Biomolecular Structure and Assembly
- Russian Foundation of Basic Research [06-04-48798]
- Division of Computing and Communication Foundations
- Direct For Computer & Info Scie & Enginr [2005209] Funding Source: National Science Foundation
The existence of three types of phenylalanyl-tRNA synthetase (PheRS), bacterial (alpha beta)(2), eukaryotic/archaeal cytosolic (alpha beta)(2), and mitochondrial alpha, is a prominent example of structural diversity within the aaRS family. PheRSs have considerably diverged in primary sequences, domain compositions, and subunit organizations. Loss of the anticodon-binding domain B8 in human cytosolic PheRS (hcPheRS) is indicative of variations in the tRNA(Phe) binding and recognition as compared to bacterial PheRSs. We report herein the crystal structure of hcPheRS in complex with phenylalanine at 3.3 angstrom resolution. A novel structural module has been revealed at the N terminus of the alpha subunit. It stretches out into the solvent of similar to 80 angstrom and is made up of three structural domains (DBDs) possessing DNA-binding fold. The dramatic reduction of aminoacylation activity for truncated N terminus variants coupled with structural data and tRNA-docking model testify that DBDs play crucial role in hcPheRS activity.
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